|
Your Input:
|
||||
| GRN | Granulins; Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling (593 aa) | |||
| CTSG | Cathepsin G; Serine protease with trypsin- and chymotrypsin-like specificity. Cleaves complement C3. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, antibacterial activity is inhibited by LPS from P.aeruginosa, Z-Gly-Leu-Phe- CH2Cl and phenylmethylsulfonyl fluoride; Belongs to the peptidase S1 family (255 aa) | |||
| GZMH | Granzyme H; Cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3’ and P4’ sites. Probably necessary for target cell lysis in cell-mediated immune responses. Participates in the antiviral response via direct cleavage of several proteins essential for viral replication (246 aa) | |||
| GZMB | Granzyme B; This enzyme is necessary for target cell lysis in cell- mediated immune responses. It cleaves after Asp. Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -7, -9 and 10 to give rise to active enzymes mediating apoptosis; Belongs to the peptidase S1 family. Granzyme subfamily (247 aa) | |||
| CTSZ | Cathepsin Z; Exhibits carboxy-monopeptidase as well as carboxy- dipeptidase activity; Cathepsins (303 aa) | |||
| CTSH | Pro-cathepsin H; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family (335 aa) | |||
| PLAT | Tissue-type plasminogen activator; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. Plays a direct role in facilitating neuronal migration (562 aa) | |||
| HGF | Hepatocyte growth factor; Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization; Deafness associated genes (728 aa) | |||
| CTSC | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII (463 aa) | |||
| CMA1 | Chymase; Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion (247 aa) | |||
| GZMM | Granzyme M; Cleaves peptide substrates after methionine, leucine, and norleucine. Physiological substrates include EZR, alpha- tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and subsequent apoptosis of target cells (257 aa) | |||
| KLKB1 | Plasma kallikrein; The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin; Belongs to the peptidase S1 family. Plasma kallikrein subfamily (638 aa) | |||
| CTSK | Cathepsin K; Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation; Cathepsins (329 aa) | |||
| PLK2 | Serine/threonine-protein kinase PLK2; Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling- required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 an [...] (685 aa) | |||
| NONO | Non-POU domain-containing octamer-binding protein; DNA- and RNA binding protein, involved in several nuclear processes. Binds the conventional octamer sequence in double-stranded DNA. Also binds single-stranded DNA and RNA at a site independent of the duplex site. Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3’ side of U5 snRNA stem 1b. Together with PSPC1, required for the formation of nuclear paraspeckles. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclea [...] (471 aa) | |||
| C21orf59 | UPF0769 protein C21orf59; Plays a role in motile cilium function, possibly by acting on outer dynein arm assembly. Seems to be important for initiation rather than maintenance of cilium motility (By similarity). Required for correct positioning of the cilium at the apical cell surface, suggesting an additional role in the planar cell polarity (PCP) pathway (By similarity). May suppress canonical Wnt signaling activity (By similarity) (290 aa) | |||
| CTSF | Cathepsin F; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis; Cathepsins (484 aa) | |||
| CTSW | Cathepsin W; May have a specific function in the mechanism or regulation of T-cell cytolytic activity; Cathepsins (376 aa) | |||
| CTSL | Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins (333 aa) | |||
| CTSB | Cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis; Cathepsins (339 aa) | |||
| WDR37 | WD repeat-containing protein 37; WD repeat domain containing (494 aa) | |||
| CTSS | Cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N; Cathepsins (331 aa) | |||
| GDF5 | Growth/differentiation factor 5; Growth factor involved in bone and cartilage formation. During cartilage development regulates differentiation of chondrogenic tissue through two pathways. Firstly, positively regulates differentiation of chondrogenic tissue through its binding of high affinity with BMPR1B and of less affinity with BMPR1A, leading to induction of SMAD1-SMAD5-SMAD8 complex phosphorylation and then SMAD protein signaling transduction. Secondly, negatively regulates chondrogenic differentiation through its interaction with NOG. Required to prevent excessive muscle loss upo [...] (501 aa) | |||
| SERPINB7 | Serpin B7; Might function as an inhibitor of Lys-specific proteases. Might influence the maturation of megakaryocytes via its action as a serpin; Serpin peptidase inhibitors (380 aa) | |||
| CTSO | Cathepsin O; Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover; Belongs to the peptidase C1 family (321 aa) | |||
| CTSV | Cathepsin L2; Cysteine protease. May have an important role in corneal physiology; Belongs to the peptidase C1 family (334 aa) | |||
